STRINGSTRING
fliC fliC yncD yncD fhuE fhuE btuB btuB pldA pldA tolC tolC exbD exbD fepA fepA acrA acrA fhuA fhuA imp imp fljB fljB
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
fliCFlagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (495 aa)
yncDSimilar to E. coli putative outer membrane receptor for iron transport (AAC74533.1); Blastp hit to AAC74533.1 (700 aa), 84% identity in aa 1 - 700. (706 aa)
fhuEOuter membrane receptor for Fe(III)-coprogen; Fe(III)-ferrioxamine B and Fe(III)-rhodotrulic acid uptake; similar to E. coli outer membrane receptor for ferric iron uptake (AAC74186.1); Blastp hit to AAC74186.1 (729 aa), 81% identity in aa 5 - 729. (724 aa)
btuBOuter membrane receptor for transport of vitamin B12, E colicins, and bacteriophage BF23; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB; Belongs to the TonB-dependent receptor family. BtuB (TC 1.B.14.3.1) subfamily. (614 aa)
pldAOuter membrane phospholipase A; Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities; Belongs to the phospholipase A1 family. (289 aa)
tolCOuter membrane channel; Specific tolerance to colicin E1; segregation of daughter chromosomes; role in organic solvent tolerance; similar to E. coli outer membrane channel; specific tolerance to colicin E1; segregation of daughter chromosomes (AAC76071.1); Blastp hit to AAC76071.1 (495 aa), 89% identity in aa 1 - 495. (491 aa)
exbDtonB-dependent uptake of B colicins; similar to E. coli uptake of enterochelin; tonB-dependent uptake of B colicins (AAC76041.1); Blastp hit to AAC76041.1 (141 aa), 93% identity in aa 1 - 141. (141 aa)
fepASimilar to E. coli outer membrane receptor for ferric enterobactin (enterochelin) and colicins B and D (AAC73685.1); Blastp hit to AAC73685.1 (746 aa), 81% identity in aa 1 - 746. (751 aa)
acrASimilar to E. coli acridine efflux pump (AAC73565.1); Blastp hit to AAC73565.1 (397 aa), 91% identity in aa 1 - 397; Belongs to the membrane fusion protein (MFP) (TC 8.A.1) family. (397 aa)
fhuAIron complex outermembrane recepter protein; Similar to E. coli outer membrane protein receptor for ferrichrome, colicin M, and phages T1, T5, and phi80 (AAC73261.1); Blastp hit to AAC73261.1 (747 aa), 68% identity in aa 1 - 747. (729 aa)
impOrganic solvent tolerance protein; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. (786 aa)
fljBFilament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (506 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.